Hainantoxin-II (HnTx-II), a novel neurotoxin, was isolated from the venom of the Chinese bird spider (Haplopelma hainanum) by cation exchange chromatography and reverse-phase HPLC. The toxin was a single chain pol...Hainantoxin-II (HnTx-II), a novel neurotoxin, was isolated from the venom of the Chinese bird spider (Haplopelma hainanum) by cation exchange chromatography and reverse-phase HPLC. The toxin was a single chain polypeptide with calculated molecular weight of 4 253.135 obtained by mass spectrometry. The complete amino acid sequence of HnTx-II was determined by Edman degradation and found to contain 37 residues with three disulfide bonds. Results showed HnTx-II can reversibly paralyze cockroaches for several hours after intra-abdominal injection with ED50 of 16 μg/g and kill the insects immediately at a dose of 60 μg/g. It was also shown to kill mice at a LD50 value of 1.41μg/g after intracerebroventricular injection. Hainantoxin-II shares 91% sequence homology with Huwentoxin-II (HwTx-II), an insecticidal peptide from another bird spider (Haplopelma schmidti) with a unique scaffold. While HnTx-II and HwTx-II both exhibit toxic activities in insects and mammals, HnTx-II shows higher insecticidal activity and lower lethiferous activity of mammals than HwTx-II. These results help clarify structural-functional relationships of the polypeptide toxin.展开更多
Poisonous organisms are represented in many taxa, including kingdom Animalia. During evolution, animals have developed special organs for production and injection of venoms. Animal venoms are complex mixtures, composi...Poisonous organisms are represented in many taxa, including kingdom Animalia. During evolution, animals have developed special organs for production and injection of venoms. Animal venoms are complex mixtures, compositions of which depend on species producing venom. The most known and studied poisonous terrestrial animals are snakes, scorpions and spiders. Among marine animals, these are jellyfishes, anemones and cone snails. The toxic substances in the venom ofthese animals are mainly of protein and peptide origin. Recent studies have indicated that the single venom may contain up to several hundred different components producing diverse physiological effects. Bites or stings by certain poisonous species result in severe envenomations leading in some cases to death. This raises the problem of bite treatment. The most effective treatment so far is the application of antivenoms. To enhance the effectiveness of such treatments, the knowledge of venom composition is needed. On the other hand, venoms contain substances with unique biological properties, which can be used both in basic science and in clinical applications. The best example of toxin application in basic science is α-bungarotoxin the discovery of which made a big impact on the studies of nicotinic acetylcholine receptor. Today compositions of venom from many species have already been examined. Based on these data, one can conclude that venoms contain a large number of individual components belonging to a limited number of structural types. Often minor changes in the amino acid sequence give rise to new biological properties. Change in the living conditions of poisonous animals lead to alterations in the composition of venoms resulting in appearance of new toxins. At the same time introduction of new methods of proteomics and genomics lead to discoveries of new compounds, which may serve as research tools or as templates for the development of novel drugs. The application of these sensitive and comprehensive methods allows studying either of venoms available in tiny amounts or of low abundant components in already known venoms.展开更多
报道了提取广西产虎纹捕鸟蛛 (Selenocosm ia huw ena) 毒素的方法。用冻干蛛毒对小鼠进行腹腔注射, 测定出虎纹捕鸟蛛毒素的LD50 为0.77 m g/kg, LD50的95% 可信限为0.72~0.82 m g/kg, 表明该毒素有很强的毒力。并观察到当用0.30 m g/...报道了提取广西产虎纹捕鸟蛛 (Selenocosm ia huw ena) 毒素的方法。用冻干蛛毒对小鼠进行腹腔注射, 测定出虎纹捕鸟蛛毒素的LD50 为0.77 m g/kg, LD50的95% 可信限为0.72~0.82 m g/kg, 表明该毒素有很强的毒力。并观察到当用0.30 m g/kg 冻干蛛毒注射小鼠颅内时, 小鼠迅速抽搐5展开更多
本文从虎纹捕鸟蛛(Selenocosmia hu wena)粗毒中经高效液相色谱分离纯化出一种组分,通过场解吸质谱(FDMS)和电子电高质谱(EIMS)鉴定为次黄嘌呤核苷,其含量为3.9%.同时,进一步用标准样品进行紫外、液相色谱对照验证,并对次黄嘌呤核苷以...本文从虎纹捕鸟蛛(Selenocosmia hu wena)粗毒中经高效液相色谱分离纯化出一种组分,通过场解吸质谱(FDMS)和电子电高质谱(EIMS)鉴定为次黄嘌呤核苷,其含量为3.9%.同时,进一步用标准样品进行紫外、液相色谱对照验证,并对次黄嘌呤核苷以毒液中的一种成分的形式存在的作用进行了简单的讨论.展开更多
基金supported by the Research Project of the Education Department of Zhejiang Province, China (Y200805989)~~
文摘Hainantoxin-II (HnTx-II), a novel neurotoxin, was isolated from the venom of the Chinese bird spider (Haplopelma hainanum) by cation exchange chromatography and reverse-phase HPLC. The toxin was a single chain polypeptide with calculated molecular weight of 4 253.135 obtained by mass spectrometry. The complete amino acid sequence of HnTx-II was determined by Edman degradation and found to contain 37 residues with three disulfide bonds. Results showed HnTx-II can reversibly paralyze cockroaches for several hours after intra-abdominal injection with ED50 of 16 μg/g and kill the insects immediately at a dose of 60 μg/g. It was also shown to kill mice at a LD50 value of 1.41μg/g after intracerebroventricular injection. Hainantoxin-II shares 91% sequence homology with Huwentoxin-II (HwTx-II), an insecticidal peptide from another bird spider (Haplopelma schmidti) with a unique scaffold. While HnTx-II and HwTx-II both exhibit toxic activities in insects and mammals, HnTx-II shows higher insecticidal activity and lower lethiferous activity of mammals than HwTx-II. These results help clarify structural-functional relationships of the polypeptide toxin.
基金Supported by The research funding from Russian Foundation for Basic Research,No.15-04-01843
文摘Poisonous organisms are represented in many taxa, including kingdom Animalia. During evolution, animals have developed special organs for production and injection of venoms. Animal venoms are complex mixtures, compositions of which depend on species producing venom. The most known and studied poisonous terrestrial animals are snakes, scorpions and spiders. Among marine animals, these are jellyfishes, anemones and cone snails. The toxic substances in the venom ofthese animals are mainly of protein and peptide origin. Recent studies have indicated that the single venom may contain up to several hundred different components producing diverse physiological effects. Bites or stings by certain poisonous species result in severe envenomations leading in some cases to death. This raises the problem of bite treatment. The most effective treatment so far is the application of antivenoms. To enhance the effectiveness of such treatments, the knowledge of venom composition is needed. On the other hand, venoms contain substances with unique biological properties, which can be used both in basic science and in clinical applications. The best example of toxin application in basic science is α-bungarotoxin the discovery of which made a big impact on the studies of nicotinic acetylcholine receptor. Today compositions of venom from many species have already been examined. Based on these data, one can conclude that venoms contain a large number of individual components belonging to a limited number of structural types. Often minor changes in the amino acid sequence give rise to new biological properties. Change in the living conditions of poisonous animals lead to alterations in the composition of venoms resulting in appearance of new toxins. At the same time introduction of new methods of proteomics and genomics lead to discoveries of new compounds, which may serve as research tools or as templates for the development of novel drugs. The application of these sensitive and comprehensive methods allows studying either of venoms available in tiny amounts or of low abundant components in already known venoms.
文摘报道了提取广西产虎纹捕鸟蛛 (Selenocosm ia huw ena) 毒素的方法。用冻干蛛毒对小鼠进行腹腔注射, 测定出虎纹捕鸟蛛毒素的LD50 为0.77 m g/kg, LD50的95% 可信限为0.72~0.82 m g/kg, 表明该毒素有很强的毒力。并观察到当用0.30 m g/kg 冻干蛛毒注射小鼠颅内时, 小鼠迅速抽搐5
文摘本文从虎纹捕鸟蛛(Selenocosmia hu wena)粗毒中经高效液相色谱分离纯化出一种组分,通过场解吸质谱(FDMS)和电子电高质谱(EIMS)鉴定为次黄嘌呤核苷,其含量为3.9%.同时,进一步用标准样品进行紫外、液相色谱对照验证,并对次黄嘌呤核苷以毒液中的一种成分的形式存在的作用进行了简单的讨论.
基金This work was supported by the National Natural Science Foundation of China (No. 30371753)the Research Project of Hebei Education Department (No. 2004110)the Doctor Foundation of Hebei Normal University (No. L2005B25)